4v0x

From Proteopedia

(Difference between revisions)

Revision as of 15:47, 27 February 2019

The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-684)

Structural highlights

4v0x is a 2 chain structure with sequence from Human and Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	4v0u, 4v0v, 4v0w
Activity:	Phosphoprotein phosphatase, with EC number 3.1.3.16
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PP1G_MOUSE] Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Dephosphorylates RPS6KB1. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E.^[1] ^[2] [PR15B_HUMAN] Maintains low levels of EIF2S1 phosphorylation in unstressed cells by promoting its dephosphorylation by PP1.

Publication Abstract from PubMed

Dephosphorylation of eukaryotic translation initiation factor 2a (eIF2a) restores protein synthesis at the waning of stress responses and requires a PP1 catalytic subunit and a regulatory subunit, PPP1R15A/GADD34 or PPP1R15B/CReP. Surprisingly, PPP1R15-PP1 binary complexes reconstituted in vitro lacked substrate selectivity. However, selectivity was restored by crude cell lysate or purified G-actin, which joined PPP1R15-PP1 to form a stable ternary complex. In crystal structures of the non-selective PPP1R15B-PP1G complex, the functional core of PPP1R15 made multiple surface contacts with PP1G, but at a distance from the active site, whereas in the substrate-selective ternary complex, actin contributes to one face of a platform encompassing the active site. Computational docking of the N-terminal lobe of eIF2a at this platform placed phosphorylated serine 51 near the active site. Mutagenesis of predicted surface-contacting residues enfeebled dephosphorylation, suggesting that avidity for the substrate plays an important role in imparting specificity on the PPP1R15B-PP1G-actin ternary complex.

G-actin provides substrate-specificity to eukaryotic initiation factor 2alpha holophosphatases.,Chen R, Rato C, Yan Y, Crespillo-Casado A, Clarke HJ, Harding HP, Marciniak SJ, Read RJ, Ron D Elife. 2015 Mar 16;4. doi: 10.7554/eLife.04871. PMID:25774600^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Schmutz I, Wendt S, Schnell A, Kramer A, Mansuy IM, Albrecht U. Protein phosphatase 1 (PP1) is a post-translational regulator of the mammalian circadian clock. PLoS One. 2011;6(6):e21325. doi: 10.1371/journal.pone.0021325. Epub 2011 Jun 21. PMID:21712997 doi:http://dx.doi.org/10.1371/journal.pone.0021325
↑ Lee HM, Chen R, Kim H, Etchegaray JP, Weaver DR, Lee C. The period of the circadian oscillator is primarily determined by the balance between casein kinase 1 and protein phosphatase 1. Proc Natl Acad Sci U S A. 2011 Sep 27;108(39):16451-6. doi:, 10.1073/pnas.1107178108. Epub 2011 Sep 19. PMID:21930935 doi:http://dx.doi.org/10.1073/pnas.1107178108
↑ Chen R, Rato C, Yan Y, Crespillo-Casado A, Clarke HJ, Harding HP, Marciniak SJ, Read RJ, Ron D. G-actin provides substrate-specificity to eukaryotic initiation factor 2alpha holophosphatases. Elife. 2015 Mar 16;4. doi: 10.7554/eLife.04871. PMID:25774600 doi:http://dx.doi.org/10.7554/eLife.04871

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4v0x"

@@ Line 3: / Line 3: @@
 <StructureSection load='4v0x' size='340' side='right' caption='[[4v0x]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4v0x]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V0X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V0X FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4v0x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V0X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V0X FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4v0u|4v0u]], [[4v0v|4v0v]], [[4v0w|4v0w]]</td></tr>
@@ Line 20: / Line 20: @@
 </div>
 <div class="pdbe-citations 4v0x" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Serine/threonine protein phosphatase|Serine/threonine protein phosphatase]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Human]]
+[[Category: Lk3 transgenic mice]]
 [[Category: Phosphoprotein phosphatase]]
 [[Category: Casado, A C]]

4v0x

From Proteopedia

Revision as of 15:47, 27 February 2019

The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-684)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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